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(Received for publication, August 30, 1995) Reduced peptide bond pseudopeptide analogues have been examined
for their ability to bind murine class I molecules of the major
histocompatibility complex (MHC). Eight pseudopeptide analogues of an
antigenic peptide derived from Plasmodium berghei (H-Ser
Volume 270,
Number 44,
Issue of November 3, 1995 pp. 26057-26059
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-Tyr-Ile-Pro-Ser-Ala-Glu-Lys-Ile
-OH)
were obtained by systematically replacing one peptide bond at a time by
a reduced peptide bond
(CH
-NH). The resulting
analogues were then tested for their binding to a recombinant single
chain SC-K
class I molecule. The comparative results show
that five analogues can efficiently mimic the parent peptide while the
introduction of the reduced bond between P3-P4, P7-P8, and
P8-P9 is deleterious for SC-K
binding. The fact that
more stable pseudopeptides containing reduced peptide bonds can bind
major histocompatibility complex molecules is of great interest for the
design of peptidomimetics with potential therapeutical properties. Such
peptide analogues may prove useful for the development of peptide-based
cytotoxic T lymphocyte vaccines.
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